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340  structures 5558  species 0  interactions 37519  sequences 456  architectures

Family: GMC_oxred_C (PF05199)

Summary: GMC oxidoreductase

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This is the Wikipedia entry entitled "Glucose-methanol-choline oxidoreductase family". More...

Glucose-methanol-choline oxidoreductase family Edit Wikipedia article

GMC oxidoreductase
PDB 3cox EBI.jpg
crystal structure of cholesterol oxidase complexed with a steroid substrate. implications for fad dependent alcohol oxidases
Identifiers
SymbolGMC_oxred_N
PfamPF00732
Pfam clanCL0063
InterProIPR000172
PROSITEPDOC00543
SCOP21gal / SCOPe / SUPFAM
GMC oxidoreductase
PDB 1coy EBI.jpg
crystal structure of cholesterol oxidase complexed with a steroid substrate. implications for fad dependent alcohol oxidases
Identifiers
SymbolGMC_oxred_C
PfamPF05199
InterProIPR007867
PROSITEPDOC00543
SCOP21gal / SCOPe / SUPFAM

In molecular biology, the glucose-methanol-choline oxidoreductase family (GMC oxidoreductase) is a family of enzymes with oxidoreductase activity.

The glucose-methanol-choline (GMC) oxidoreductases are FAD flavoproteins oxidoreductases.[1][2] These enzymes include a variety of proteins; choline dehydrogenase (CHD) EC 1.1.99.1, methanol oxidase (MOX) EC 1.1.3.13 and cellobiose dehydrogenase EC 1.1.99.18[3] which share a number of regions of sequence similarities. They contain two conserved protein domains. The N-terminal domain corresponds to the FAD ADP-binding domain, the C-terminal domain is a steroid-biding domain.[4][5]


References

  1. ^ Cavener DR (1992). "GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities". J. Mol. Biol. 223 (3): 811–4. PMID 1542121. {{cite journal}}: Unknown parameter |month= ignored (help)
  2. ^ Li J, Vrielink A, Brick P, Blow DM (1993). "Crystal structure of cholesterol oxidase complexed with a steroid substrate: implications for flavin adenine dinucleotide dependent alcohol oxidases". Biochemistry. 32 (43): 11507–15. PMID 8218217. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  3. ^ Henriksson G, Johansson G, Pettersson G (2000). "A critical review of cellobiose dehydrogenases". J. Biotechnol. 78 (2): 93–113. PMID 10725534. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  4. ^ Bannwarth M, Bastian S, Heckmann-Pohl D, Giffhorn F, Schulz GE (2004). "Crystal structure of pyranose 2-oxidase from the white-rot fungus Peniophora sp". Biochemistry. 43 (37): 11683–90. doi:10.1021/bi048609q. PMID 15362852.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  5. ^ Vrielink A, Lloyd LF, Blow DM (1991). "Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 A resolution". J Mol Biol. 219 (3): 533–54. PMID 2051487.{{cite journal}}: CS1 maint: multiple names: authors list (link)
This article incorporates text from the public domain Pfam and InterPro: IPR000172
This article incorporates text from the public domain Pfam and InterPro: IPR007867

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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GMC oxidoreductase Provide feedback

This domain found associated with PF00732.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR007867

The glucose-methanol-choline (GMC) oxidoreductases are FAD flavoproteins oxidoreductases [ PUBMED:1542121 , PUBMED:8218217 ]. These enzymes include a variety of proteins; choline dehydrogenase (CHD), methanol oxidase (MOX) and cellobiose dehydrogenase ( EC ) [ PUBMED:10725534 ] which share a number of regions of sequence similarities. The function of this C-terminal conserved domain is not yet known.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(75)
Full
(37519)
Representative proteomes UniProt
(118501)
RP15
(5030)
RP35
(16656)
RP55
(33383)
RP75
(56001)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

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  Seed
(75)
Full
(37519)
Representative proteomes UniProt
(118501)
RP15
(5030)
RP35
(16656)
RP55
(33383)
RP75
(56001)
Alignment:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(75)
Full
(37519)
Representative proteomes UniProt
(118501)
RP15
(5030)
RP35
(16656)
RP55
(33383)
RP75
(56001)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_891 (release 2.1)
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Studholme DJ , Bateman A
Number in seed: 75
Number in full: 37519
Average length of the domain: 133.8 aa
Average identity of full alignment: 24 %
Average coverage of the sequence by the domain: 22.91 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 24.4 24.4
Trusted cut-off 24.4 24.4
Noise cut-off 24.3 24.3
Model length: 145
Family (HMM) version: 16
Download: download the raw HMM for this family

Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the GMC_oxred_C domain has been found. There are 340 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A044TLX6 View 3D Structure Click here
A0A075TRK9 View 3D Structure Click here
A0A077YV93 View 3D Structure Click here
A0A0A2V3B7 View 3D Structure Click here
A0A0D2DCZ4 View 3D Structure Click here
A0A0D2DRI8 View 3D Structure Click here
A0A0D2DW81 View 3D Structure Click here
A0A0D2EK50 View 3D Structure Click here
A0A0D2F820 View 3D Structure Click here
A0A0D2FEL7 View 3D Structure Click here
A0A0D2G637 View 3D Structure Click here
A0A0D2G8R3 View 3D Structure Click here
A0A0D2GIJ2 View 3D Structure Click here
A0A0D2GSG2 View 3D Structure Click here
A0A0D2GSV3 View 3D Structure Click here
A0A0D2GTE0 View 3D Structure Click here
A0A0D2GUY0 View 3D Structure Click here
A0A0D2H716 View 3D Structure Click here
A0A0D2HC52 View 3D Structure Click here
A0A0D2HIC9 View 3D Structure Click here
A0A0D2HL33 View 3D Structure Click here
A0A0H3GL29 View 3D Structure Click here
A0A0H3GPC6 View 3D Structure Click here
A0A0K0ES56 View 3D Structure Click here
A0A0N7KGH1 View 3D Structure Click here
A0A0N7KMI8 View 3D Structure Click here
A0A0P0VMX7 View 3D Structure Click here
A0A0P0XV74 View 3D Structure Click here
A0A0P0XVN3 View 3D Structure Click here
A0A0P0XVX1 View 3D Structure Click here
A0A0R0HV52 View 3D Structure Click here
A0A0R0HY57 View 3D Structure Click here
A0A0R0J8L5 View 3D Structure Click here
A0A0R0KVH3 View 3D Structure Click here
A0A0R0LG50 View 3D Structure Click here
A0A150ASY8 View 3D Structure Click here
A0A158Q4G7 View 3D Structure Click here
A0A175VNF2 View 3D Structure Click here
A0A175VP38 View 3D Structure Click here
A0A175VPT5 View 3D Structure Click here